Toda H, Yazawa M, Kondo K, Honma T, Narita K, Yagi K
J Biochem. 1981 Nov;90(5):1493-505. doi: 10.1093/oxfordjournals.jbchem.a133616.
The complete amino acid sequence of scallop calmodulin was determined by isolating and sequencing the peptides obtained after cyanogen bromide cleavage and tryptic digestion. The protein consisted of 148 amino acid residues and its amino(N)-terminus was blocked with an acetyl group. Scallop calmodulin lacked tryptophan and cysteine residues and contained one mol each of N epsilon-trimethyllysine (Tml) and histidine residues per mol of the protein. Scallop calmodulin contained only one tyrosine residue, while vertebrate calmodulins contain two. On comparing its amino acid sequence with that of bovine calmodulin, three amino acid substitutions were found at positions 99(Tyr leads to Phe), 143(Gln leads to Thr), and 147(Ala leads to Ser).
通过分离和测序溴化氰裂解及胰蛋白酶消化后得到的肽段，确定了扇贝钙调蛋白的完整氨基酸序列。该蛋白质由148个氨基酸残基组成，其氨基（N）末端被乙酰基封闭。扇贝钙调蛋白缺乏色氨酸和半胱氨酸残基，每摩尔蛋白质含有1摩尔的Nε-三甲基赖氨酸（Tml）和组氨酸残基。扇贝钙调蛋白仅含有一个酪氨酸残基，而脊椎动物钙调蛋白含有两个。将其氨基酸序列与牛钙调蛋白的序列进行比较，发现在第99位（酪氨酸变为苯丙氨酸）、143位（谷氨酰胺变为苏氨酸）和147位（丙氨酸变为丝氨酸）有三个氨基酸替换。
